Nanoscale organization and function of proteins at the centriole-cilium interface
Abstract/Contents
- Abstract
- Centrioles are conserved organelles comprised of nine-fold symmetric triplet microtubules. In animal cells, centrioles organize microtubule structures such as the mitotic spindle, the primary cilium and motile cilia. The primary cilium is required for proper cellular signaling. Motile cilia are involved in movement of extracellular material or cellular motility. While the ultrastructure of centrioles and cilia has been well studied using electron microscopy, the distribution of specific proteins at centrioles has been harder to investigate due to the small size of the centriole, near the diffraction limit of light microscopy. STED (stimulated emission depletion) and 3D- SIM (three dimensional structured illumination microscopy) super-resolution imaging was used to determine the nine-fold symmetric distribution of the centriolar distal appendage protein Cep164 and the organization of several other centriole distal end proteins involved in cilium function, including Cby1, Ahi1 and Ofd1. Cby1, which co- localizes in a centriolar subdomain with Ahi1 and Ofd1, was found to be required for efficient primary cilium formation and function. Loss of Cby1 results in cystic kidneys in a mouse model and reduced recruitment of the Joubert syndrome gene product Arl13b to the primary cilium. Localization of Ahi1, also a Joubert syndrome gene product, to the centriolar transition zone is impaired in cells lacking Cby1. These data suggest Cby1 is required for proper assembly of the transition zone, which is in turn required for efficient ciliogenesis and regulation of ciliary content. Cby1 likely represents a component of a molecular anchor at the mature centriole for the assembly of ciliary transition zone components.
Description
| Type of resource | text |
|---|---|
| Form | electronic; electronic resource; remote |
| Extent | 1 online resource. |
| Publication date | 2014 |
| Issuance | monographic |
| Language | English |
Creators/Contributors
| Associated with | Lee, Yin Loon |
|---|---|
| Associated with | Stanford University, Department of Biology. |
| Primary advisor | Stearns, Tim |
| Thesis advisor | Stearns, Tim |
| Thesis advisor | Kopito, Ron Rieger |
| Thesis advisor | Nelson, William J, Jr |
| Advisor | Kopito, Ron Rieger |
| Advisor | Nelson, William J, Jr |
Subjects
| Genre | Theses |
|---|
Bibliographic information
| Statement of responsibility | Yin Loon Lee. |
|---|---|
| Note | Submitted to the Department of Biology. |
| Thesis | Thesis (Ph.D.)--Stanford University, 2014. |
| Location | electronic resource |
Access conditions
- Copyright
- © 2014 by Yin Loon Lee
- License
- This work is licensed under a Creative Commons Attribution Non Commercial 3.0 Unported license (CC BY-NC).
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